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Results 1 - 10 of 18 > >>
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EC Number Cofactor Commentary Reference
Show all pathways known for 1.3.1.10Display the word mapDisplay the reaction diagram Show all sequences 1.3.1.10FAD enzyme contains 0.8 mol FAD/enzyme, but functional role is not investigated 390508
Show all pathways known for 1.3.1.10Display the word mapDisplay the reaction diagram Show all sequences 1.3.1.10FMN - 726431, 762574
Show all pathways known for 1.3.1.10Display the word mapDisplay the reaction diagram Show all sequences 1.3.1.10more enzyme also exhibits NADPH dependent activity, if isolated at pH 6.5 390503
Show all pathways known for 1.3.1.10Display the word mapDisplay the reaction diagram Show all sequences 1.3.1.10more enzyme is highly specific for NADH, even if isolated at pH 6.5 390504
Show all pathways known for 1.3.1.10Display the word mapDisplay the reaction diagram Show all sequences 1.3.1.10NADH - 740013, 740716
Show all pathways known for 1.3.1.10Display the word mapDisplay the reaction diagram Show all sequences 1.3.1.10NADH also essential for activity, article leaves doubtful whether NADH or NADPH or both are cofactors 390508
Show all pathways known for 1.3.1.10Display the word mapDisplay the reaction diagram Show all sequences 1.3.1.10NADH poor cofactor 726431
Show all pathways known for 1.3.1.10Display the word mapDisplay the reaction diagram Show all sequences 1.3.1.10NADP+ dependent 684170
Show all pathways known for 1.3.1.10Display the word mapDisplay the reaction diagram Show all sequences 1.3.1.10NADP+ FabL is NADP+-dependent, the side chain of Lys164 of the Tyr-(Xaa)6-Lys dyad at the active site forms a hydrogen bond with the hydroxyl group of the nicotinamide ribose moiety, binding structure, overview 711113
Show all pathways known for 1.3.1.10Display the word mapDisplay the reaction diagram Show all sequences 1.3.1.10NADP+ the side chain of Lys164 of the Tyr-(Xaa)6-Lys dyad at the active site forms a hydrogen bond with the hydroxyl group of the nicotinamide ribose moiety, binding structure, overview 711113
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